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Literature summary for 3.5.3.11 extracted from

  • Goda, S.; Sakuraba, H.; Kawarabayasi, Y.; Ohshima, T.
    The first archaeal agmatinase from anaerobic hyperthermophilic archaeon Pyrococcus horikoshii: cloning, expression, and characterization (2005), Biochim. Biophys. Acta, 1748, 110-115.
    View publication on PubMed
Search for more literature for 3.5.3.11

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli. Mainly obtained as inactive inclusion body in Escherichia coli Pyrococcus horikoshii

Inhibitors

Inhibitors Comment Organism Structure
putrescine
-
 Pyrococcus horikoshii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.53
-
 agmatine 50°C, pH 11.3 Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2 Pyrococcus horikoshii
Co2+ enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2 Pyrococcus horikoshii
Mg2+ enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2 Pyrococcus horikoshii
Mn2+ enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2 Pyrococcus horikoshii
Zn2+ enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2 Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31000
-
 4 * 31000, SDS-PAGE Pyrococcus horikoshii
145000
-
 gel filtration Pyrococcus horikoshii

Organic Solvent Stability

Organic Solvent Comment Organism
dimethyl sulfoxide 10%, no loss of activity at 50°C Pyrococcus horikoshii
Ethanol 10%, no loss of activity at 50°C Pyrococcus horikoshii
Methanol 10%, no loss of activity at 50°C Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
agmatine + H2O
-
 Pyrococcus horikoshii putrescine + urea
-
 ?
additional information no activity with arginine Pyrococcus horikoshii ?
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 31000, SDS-PAGE Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
100
-
-
 Pyrococcus horikoshii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
 10 min, stable Pyrococcus horikoshii
90
-
 10 min, 53% loss of activity Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
11
-
-
 Pyrococcus horikoshii

pH Range

pH Minimum pH Maximum Comment Organism
9.5 12.5 pH 9.5: about 50% of maximal activity, pH 12.5: about 85% of maximal activity Pyrococcus horikoshii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.8
-
 putrescine 50°C, pH 11.3 Pyrococcus horikoshii